ID   VL1_HPV56               Reviewed;         534 AA.
AC   P36743; Q90082;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-JUN-2021, entry version 86.
DE   RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS   Human papillomavirus 56.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10596;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA   Delius H., Hofmann B.;
RT   "Primer-directed sequencing of human papillomavirus types.";
RL   Curr. Top. Microbiol. Immunol. 186:13-31(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 371-402.
RX   PubMed=1321168; DOI=10.1128/jcm.30.7.1716-1721.1992;
RA   van den Brule A.J., Snijders P.J., Raaphorst P.M., Schrijnemakers H.F.,
RA   Delius H., Gissmann L., Meijer C.J., Walboomers J.M.;
RT   "General primer polymerase chain reaction in combination with sequence
RT   analysis for identification of potentially novel human papillomavirus
RT   genotypes in cervical lesions.";
RL   J. Clin. Microbiol. 30:1716-1721(1992).
CC   -!- FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 50 nm
CC       diameter. The capsid is composed of 72 pentamers linked to each other
CC       by disulfide bonds and associated with L2 proteins. Binds to heparan
CC       sulfate proteoglycans on cell surface of basal layer keratinocytes to
CC       provide initial virion attachment. This binding mediates a
CC       conformational change in the virus capsid that facilitates efficient
CC       infection. The virion enters the host cell via endocytosis. During
CC       virus trafficking, L1 protein dissociates from the viral DNA and the
CC       genomic DNA is released to the host nucleus. The virion assembly takes
CC       place within the cell nucleus. Encapsulates the genomic DNA together
CC       with protein L2. {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SUBUNIT: Self-assembles into homopentamers. The capsid has an
CC       icosahedral symmetry and consists of 72 capsomers, with each capsomer
CC       being a pentamer of L1. Interacts with the minor capsid protein L2;
CC       this interaction is necessary for viral genome encapsidation. Interacts
CC       with protein E2; this interaction enhances E2-dependent replication and
CC       transcription activation. {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04002}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae L1 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04002}.
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DR   EMBL; X74483; CAA52600.1; -; Genomic_DNA.
DR   EMBL; S40273; AAB22569.1; -; Genomic_DNA.
DR   PIR; S36583; S36583.
DR   SMR; P36743; -.
DR   PRIDE; P36743; -.
DR   Proteomes; UP000007666; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.175.20; -; 2.
DR   HAMAP; MF_04002; PPV_L1; 1.
DR   InterPro; IPR002210; Capsid_L1_Papillomavir.
DR   InterPro; IPR036973; Capsid_L1_sf_Papillomavir.
DR   InterPro; IPR011222; dsDNA_vir_gr_I_capsid.
DR   Pfam; PF00500; Late_protein_L1; 1.
DR   PRINTS; PR00865; HPVCAPSIDL1.
DR   SUPFAM; SSF88648; SSF88648; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Disulfide bond; Host nucleus; Host-virus interaction;
KW   Late protein; Reference proteome; T=7 icosahedral capsid protein;
KW   Viral attachment to host cell; Viral penetration into host cytoplasm;
KW   Virion; Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..534
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133539"
FT   REGION          508..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        209
FT                   /note="Interchain (with C-461)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        461
FT                   /note="Interchain (with C-209)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   534 AA;  60161 MW;  2ED3A965D1B1EC96 CRC64;
     MMLPMMYIYR DPPLHYGLCI FLDVGAVNVF PIFLQMATWR PSENKVYLPP TPVSKVVATD
     SYVKRTSIFY HAGSSRLLAV GHPYYSVTKD NTKTNIPKVS AYQYRVFRVR LPDPNKFGLP
     DTNIYNPDQE RLVWACVGLE VGRGQPLGAG LSGHPLFNRL DDTESSNLAN NNVIEDSRDN
     ISVDGKQTQL CIVGCTPAMG EHWTKGAVCK STQVTTGDCP PLALINTPIE DGDMIDTGFG
     AMDFKVLQES KAEVPLDIVQ STCKYPDYLK MSADAYGDSM WFYLRREQLF ARHYFNRAGK
     VGETIPAELY LKGSNGREPP PSSVYVATPS GSMITSEAQL FNKPYWLQRA QGHNNGICWG
     NQLFVTVVDT TRSTNMTIST ATEQLSKYDA RKINQYLRHV EEYELQFVFQ LCKITLSAEV
     MAYLHNMNAN LLEDWNIGLS PPVATSLEDK YRYVRSTAIT CQREQPPTEK QDPLAKYKFW
     DVNLQDSFST DLDQFPLGRK FLMQLGTRSK PAVATSKKRS APTSTSTPAK RKRR